The genomic structure and predicted protein structure encoded by mouse and human Clec9A genes. (A) Protein sequence alignment of the predicted protein sequence of mouse and human Clec9A. Sequence identity is highlighted in dark gray, similarity is shown in light gray. Invariant residues are shown in bold. Exon boundaries are denoted by . (B) Schematic representation of the gene structures of mClec9A and hCLEC9A, determined by alignment of the cDNA to the genomic sequence databases of the C57BL/6J mouse and human databases, respectively. Exons encoding the coding region of Clec9A genes are denoted by black boxes and the size (bp) of the exons and introns are shown below. (C) A schematic representation of the mouse and human Clec9A proteins. Pins denote potential N-glycosylation sites. (D) Alignment of the CTLD of mouse and human Clec9A to proteins that share sequence homology. Rat mannose binding protein A (MBP-A) is included for comparison as a classical C-type lectin domain that has functional carbohydrate recognition domains. Gray boxes indicate conserved residues, + indicates additional pair of cysteine residues involved in protein homodimeration, and * marks the conserved cysteine residues that form disulfide bonds. The residues that ligate Ca²⁺ in the MBP-A are designated 1 and 2.